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PEX2_MOUSE
ID   PEX2_MOUSE              Reviewed;         305 AA.
AC   P55098; O35467;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 150.
DE   RecName: Full=Peroxisome biogenesis factor 2;
DE   AltName: Full=Peroxin-2;
DE   AltName: Full=Peroxisomal membrane protein 3;
DE   AltName: Full=Peroxisome assembly factor 1;
DE            Short=PAF-1;
GN   Name=Pex2; Synonyms=Paf1, Pmp35, Pxmp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Swiss Webster; TISSUE=Liver;
RX   PubMed=8043297; DOI=10.1006/bmmb.1994.1018;
RA   Wilson G.N., Bryant D.D.;
RT   "Structure and expression of mammalian peroxisome assembly factor-1 (PMP35)
RT   genes.";
RL   Biochem. Med. Metab. Biol. 51:140-148(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=9382874; DOI=10.1083/jcb.139.5.1293;
RA   Faust P.L., Hatten M.E.;
RT   "Targeted deletion of the PEX2 peroxisome assembly gene in mice provides a
RT   model for Zellweger syndrome, a human neuronal migration disorder.";
RL   J. Cell Biol. 139:1293-1305(1997).
CC   -!- FUNCTION: Somewhat implicated in the biogenesis of peroxisomes.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {ECO:0000305}.
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DR   EMBL; L27842; AAA21742.1; -; Genomic_DNA.
DR   EMBL; AF031128; AAB91465.1; -; mRNA.
DR   PIR; I52362; I52362.
DR   RefSeq; NP_001156773.1; NM_001163301.2.
DR   RefSeq; NP_001156774.1; NM_001163302.2.
DR   RefSeq; NP_001156777.1; NM_001163305.2.
DR   RefSeq; NP_001156778.1; NM_001163306.2.
DR   RefSeq; NP_001254643.1; NM_001267714.1.
DR   RefSeq; NP_001254644.1; NM_001267715.1.
DR   RefSeq; NP_033020.2; NM_008994.4.
DR   RefSeq; XP_006530121.1; XM_006530058.3.
DR   RefSeq; XP_006530122.1; XM_006530059.2.
DR   RefSeq; XP_011246442.1; XM_011248140.2.
DR   RefSeq; XP_017174994.1; XM_017319505.1.
DR   AlphaFoldDB; P55098; -.
DR   BioGRID; 202524; 1.
DR   IntAct; P55098; 2.
DR   MINT; P55098; -.
DR   STRING; 10090.ENSMUSP00000071255; -.
DR   PhosphoSitePlus; P55098; -.
DR   MaxQB; P55098; -.
DR   PRIDE; P55098; -.
DR   ProteomicsDB; 289473; -.
DR   DNASU; 19302; -.
DR   GeneID; 19302; -.
DR   KEGG; mmu:19302; -.
DR   CTD; 5828; -.
DR   MGI; MGI:107486; Pex2.
DR   eggNOG; KOG2879; Eukaryota.
DR   InParanoid; P55098; -.
DR   OrthoDB; 1494604at2759; -.
DR   PhylomeDB; P55098; -.
DR   BioGRID-ORCS; 19302; 10 hits in 72 CRISPR screens.
DR   ChiTaRS; Pex2; mouse.
DR   PRO; PR:P55098; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P55098; protein.
DR   GO; GO:0016593; C:Cdc73/Paf1 complex; ISO:MGI.
DR   GO; GO:0005779; C:integral component of peroxisomal membrane; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR   GO; GO:0005777; C:peroxisome; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006699; P:bile acid biosynthetic process; IMP:MGI.
DR   GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0007031; P:peroxisome organization; ISO:MGI.
DR   GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR   GO; GO:0016558; P:protein import into peroxisome matrix; ISO:MGI.
DR   GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IMP:MGI.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:MGI.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR006845; Pex_N.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF04757; Pex2_Pex12; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Metal-binding; Peroxisome; Peroxisome biogenesis;
KW   Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN           1..305
FT                   /note="Peroxisome biogenesis factor 2"
FT                   /id="PRO_0000056370"
FT   TRANSMEM        140..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         244..284
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   CONFLICT        1..8
FT                   /note="MAAREEST -> MTGKEENM (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="H -> Y (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91..94
FT                   /note="PNPV -> LNLI (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="N -> T (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="L -> W (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114
FT                   /note="R -> K (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="C -> F (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        142
FT                   /note="V -> L (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="M -> I (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225..227
FT                   /note="TLC -> IPL (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="A -> S (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="Q -> E (in Ref. 2; AAB91465)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   305 AA;  34732 MW;  FAFB6C8913F959F0 CRC64;
     MAAREESTQS ANRVLRISQL DALELNKALE QLVWSQFTQC FHGFKPGLLA RFEPEVKAFL
     WLFLWRFTIY SKNATVGQSV LNIQHKNDSS PNPVYQPPSK NQKLLYAVCT IGGRWLEERC
     YDLFRNRHLA SFGKAKQCMN FVVGLLKLGE LMNFLIFLQK GKFATLTERL LGIHSVFCKP
     QNMREVGFEY MNRELLWHGF AEFLIFLLPL INIQKLKAKL SSWCTLCTGA AGHDSTLGSS
     GKECALCGEW PTMPHTIGCE HVFCYYCVKS SFLFDIYFTC PKCGTEVHSV QPLKAGIQMS
     EVNAL
 
 
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